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P17066 (HSP76_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 6
Alternative name(s):
Heat shock 70 kDa protein B'
Gene names
Name:HSPA6
Synonyms:HSP70B'
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length643 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage By similarity.

Induction

Only at higher temperatures, and no basal expression.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to unfolded protein

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 643643Heat shock 70 kDa protein 6
PRO_0000078264

Natural variations

Natural variant651P → T. Ref.2
VAR_060718
Natural variant951R → Q. Ref.2
VAR_060719
Natural variant1501A → T. Ref.2
Corresponds to variant rs10919224 [ dbSNP | Ensembl ].
VAR_049605
Natural variant1531N → S. Ref.2
Corresponds to variant rs10919225 [ dbSNP | Ensembl ].
VAR_049606
Natural variant1541D → N. Ref.2
Corresponds to variant rs10919226 [ dbSNP | Ensembl ].
VAR_049607
Natural variant1591A → V. Ref.2
VAR_060720
Natural variant1701N → K. Ref.2
Corresponds to variant rs41297704 [ dbSNP | Ensembl ].
VAR_049608
Natural variant1731R → P. Ref.2
Corresponds to variant rs41297708 [ dbSNP | Ensembl ].
VAR_049609
Natural variant1781P → A. Ref.2
Corresponds to variant rs41297710 [ dbSNP | Ensembl ].
VAR_049610
Natural variant1941E → K. Ref.2
Corresponds to variant rs41297714 [ dbSNP | Ensembl ].
VAR_049611
Natural variant1981L → F. Ref.2
Corresponds to variant rs1079109 [ dbSNP | Ensembl ].
VAR_024182
Natural variant2601R → H.
Corresponds to variant rs41299256 [ dbSNP | Ensembl ].
VAR_049612
Natural variant2971T → K. Ref.2
VAR_060721
Natural variant3361V → F.
Corresponds to variant rs417707 [ dbSNP | Ensembl ].
VAR_059360
Natural variant4641S → I. Ref.2
Corresponds to variant rs388218 [ dbSNP | Ensembl ].
VAR_049613
Natural variant4711R → H. Ref.2
Corresponds to variant rs41299256 [ dbSNP | Ensembl ].
VAR_049614
Natural variant5281K → E. Ref.2
Corresponds to variant rs570189 [ dbSNP | Ensembl ].
VAR_049615
Natural variant5281K → R.
Corresponds to variant rs570167 [ dbSNP | Ensembl ].
VAR_059361
Natural variant5621D → E. Ref.2
Corresponds to variant rs753856 [ dbSNP | Ensembl ].
VAR_024183
Natural variant5721M → V.
Corresponds to variant rs452004 [ dbSNP | Ensembl ].
VAR_049616
Natural variant5771R → Q. Ref.2
Corresponds to variant rs368844 [ dbSNP | Ensembl ].
VAR_049617
Natural variant6261T → A. Ref.2
Corresponds to variant rs41299260 [ dbSNP | Ensembl ].
VAR_049618

Experimental info

Sequence conflict106 – 1083RVC → PVS Ref.1
Sequence conflict106 – 1083RVC → PVS Ref.3
Sequence conflict2631R → G in CAA36061. Ref.1

Secondary structure

.................................................................... 643
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17066 [UniParc].

Last modified September 19, 2003. Version 2.
Checksum: BCE348F0226DB70B

FASTA64371,028
        10         20         30         40         50         60 
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE RLVGDAAKSQ 

        70         80         90        100        110        120 
AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG GKPKVRVCYR GEDKTFYPEE 

       130        140        150        160        170        180 
ISSMVLSKMK ETAEAYLGQP VKHAVITVPA YFNDSQRQAT KDAGAIAGLN VLRIINEPTA 

       190        200        210        220        230        240 
AAIAYGLDRR GAGERNVLIF DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV 

       250        260        270        280        290        300 
NHFMEEFRRK HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT 

       310        320        330        340        350        360 
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK LLQDFFNGKE 

       370        380        390        400        410        420 
LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP LSLGLETAGG VMTTLIQRNA 

       430        440        450        460        470        480 
TIPTKQTQTF TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF 

       490        500        510        520        530        540 
DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA 

       550        560        570        580        590        600 
KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE 

       610        620        630        640 
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD 

« Hide

References

« Hide 'large scale' references
[1]"The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA."
Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.
Biochem. J. 267:125-132(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Lung.
[2]NIEHS SNPs program
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-65; GLN-95; THR-150; SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178; LYS-194; PHE-198; LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577 AND ALA-626.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary and Skin.
[5]"The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1."
Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.
Genomics 12:74-79(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
[6]"Cis-acting elements involved in the regulated expression of a human HSP70 gene."
Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.
J. Mol. Biol. 203:97-105(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.
IPIIPI00339269.
PIRS09036.
RefSeqNP_002146.2. NM_002155.3.
UniGeneHs.654614.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE1X-ray2.20A/B/C6-385[»]
ProteinModelPortalP17066.
ModBaseSearch...

Protein-protein interaction databases

IntActP17066. 19 interactions.
MINTMINT-1139180.
STRING9606.ENSP00000310219.

PTM databases

PhosphoSiteP17066.

Polymorphism databases

DMDM34978357.

2D gel databases

UCD-2DPAGEP17066.

Proteomic databases

PaxDbP17066.
PRIDEP17066.

Protocols and materials databases

DNASU3310.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309758; ENSP00000310219; ENSG00000173110.
GeneID3310.
KEGGhsa:3310.
UCSCuc001gaq.3. human.

Organism-specific databases

CTD3310.
GeneCardsGC01P161495.
HGNCHGNC:5239. HSPA6.
HPACAB017452.
HPA028549.
MIM140555. gene.
neXtProtNX_P17066.
PharmGKBPA29505.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP17066.
KOK03283.
OMALEAYVFH.
OrthoDBEOG4Q58P1.
PhylomeDBP17066.

Gene expression databases

BgeeP17066.
CleanExHS_HSPA6.
GenevestigatorP17066.
GermOnlineENSG00000173110. Homo sapiens.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17066.
GenomeRNAi3310.
NextBio13127.
SOURCESearch...

Entry information

Entry nameHSP76_HUMAN
AccessionPrimary (citable) accession number: P17066
Secondary accession number(s): Q1HBA8, Q8IYK7, Q9BT95
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 19, 2003
Last modified: May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families